. Author manuscript; available in PMC: 2018 May 4.

Published in final edited form as: J Med Chem. 2016 Dec 21;60(4):1262–1271. doi: 10.1021/acs.jmedchem.6b00990

Table 1.

Kinetic Parameters of PARP Full Length Enzymes and Catalytic Domain Fragments^a

protein	construct	K_M^NAD+(μM)	K_M^NAD+ (literature)
PARP1	FL	0.78 ± 0.45	50 μM⁶²
PARP1	ART	94 ± 27	30−130 μM^63–66
PARP2	FL	1.9 ± 0.5	130 μM⁶⁵
PARP2	ART	159 ± 5
PARP3	FL	131 ± 57
PARP3	ART	2170 ± 645
PARP4	ART	92 ± 17
TNKS1	ART	31 ± 4
TNKS2	ART	251 ± 56
PARP10	FL	98 ± 11	50 μM⁶⁷
PARP10	ART	90 ± 27
PARP12	ART	299 ± 76
PARP14	ART	62 ± 7
PARP15	ART	11.0 ± 4.2
PARP16	FL	582 ± 196	280 μM^68,69

Experimental data are shown in Supporting Information, Figure S2. FL, full length protein; ART, ADP-ribosyltransferase domain including the regulatory subdomain (in PARP1−4).